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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Psychrobacter cryohalolentis (strain K5)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.UniRule annotation

Catalytic activityi

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.UniRule annotation
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.UniRule annotation
(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA.UniRule annotation
(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.UniRule annotation

Pathway: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei120 – 1201Important for catalytic activityUniRule annotation
Sitei140 – 1401Important for catalytic activityUniRule annotation
Binding sitei298 – 2981SubstrateUniRule annotation
Binding sitei326 – 3261NAD; via amide nitrogenUniRule annotation
Binding sitei345 – 3451NADUniRule annotation
Binding sitei409 – 4091NADUniRule annotation
Active sitei452 – 4521For 3-hydroxyacyl-CoA dehydrogenase activityUniRule annotation
Binding sitei455 – 4551NADUniRule annotation
Binding sitei502 – 5021SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi402 – 4043NADUniRule annotation
Nucleotide bindingi429 – 4313NADUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid degradation, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciPCRY335284:GHE9-2271-MONOMER.
UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid oxidation complex subunit alphaUniRule annotation
Including the following 2 domains:
Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimeraseUniRule annotation (EC:4.2.1.17UniRule annotation, EC:5.1.2.3UniRule annotation, EC:5.3.3.8UniRule annotation)
3-hydroxyacyl-CoA dehydrogenaseUniRule annotation (EC:1.1.1.35UniRule annotation)
Gene namesi
Name:fadBUniRule annotation
Ordered Locus Names:Pcryo_2227
OrganismiPsychrobacter cryohalolentis (strain K5)
Taxonomic identifieri335284 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter
ProteomesiUP000002425 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 719719Fatty acid oxidation complex subunit alphaPRO_0000255844Add
BLAST

Interactioni

Subunit structurei

Heterotetramer of two alpha chains (FadB) and two beta chains (FadA).UniRule annotation

Protein-protein interaction databases

STRINGi335284.Pcryo_2227.

Structurei

3D structure databases

ProteinModelPortaliQ1Q8J9.
SMRiQ1Q8J9. Positions 1-717.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 190190Enoyl-CoA hydratase/isomeraseUniRule annotationAdd
BLAST
Regioni313 – 7194073-hydroxyacyl-CoA dehydrogenaseUniRule annotationAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.UniRule annotation
In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000261344.
KOiK01825.
OMAiNWLEDGI.
OrthoDBiEOG6M9F0M.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
HAMAPiMF_01621. FadB.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR02437. FadB. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q1Q8J9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVYQGNRITV TMLEDGIANM QYNAENESVN KFDTETNKQF AEVVNALEKA
60 70 80 90 100
DDIKGLIVTS SKGVFIAGAD ITEFVASFKQ SEEEIKDWVI NINDAFNRFE
110 120 130 140 150
DLPFPKVAAI NGAALGGGCE MTLVCEYRVM SDKAIIGLPE TQLGIFPGFG
160 170 180 190 200
GTVRSTRVIG IDNALELIAT GTPKKALDAL KLGLVDATVA ADDLQDAAID
210 220 230 240 250
LVKKCISDEL DWQAKREEKL VPVKLNQLEQ AMAFNSAKGM IFAKANPKQY
260 270 280 290 300
PAPALAIAAI EKHVNLPRDK AIEVEAAGFA KAAKTPQAES LVGLFLSDQL
310 320 330 340 350
VKKLAKQHSK KAHDINEAAV LGAGIMGGGI AYQAASKGLP IIMKDIKSEQ
360 370 380 390 400
LDLGMGEASK LLGKMVDRGK ITPAKMGETL SRIRPTLNYG DFAETDIVIE
410 420 430 440 450
AVVENPNVKR AVLKEVEGLV KDDCILASNT STISITFLAE ALERPENFVG
460 470 480 490 500
MHFFNPVNRM PLVEVIRGEK SSEEAISTTV ALATKMGKVP VVVNDCPGFL
510 520 530 540 550
VNRVLFPYFG AFDLLLKQGA DFAHVDKVME KFGWPMGPAY LIDVVGLDTG
560 570 580 590 600
VHGAEVMAEG FPDRMKPDYK GAIEHLYENK RLGQKNGVGF YKYEMDKRGK
610 620 630 640 650
PKKVADEATY ELLKTTTDSD KQTFEDQAII DRTMLAFCNE TVRCLEDNIV
660 670 680 690 700
STPSEADMAM IMGVGFPPFR GGPCRYIDQM GLDNYLALCE KYAYLGKAYE
710
APQKIRDMAA AGETFYATA
Length:719
Mass (Da):78,378
Last modified:May 16, 2006 - v1
Checksum:i0A15859CAFCD9966
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000323 Genomic DNA. Translation: ABE76004.1.
RefSeqiWP_011514537.1. NC_007969.1.
YP_581488.1. NC_007969.1.

Genome annotation databases

EnsemblBacteriaiABE76004; ABE76004; Pcryo_2227.
KEGGipcr:Pcryo_2227.
PATRICi23064087. VBIPsyCry128170_2356.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000323 Genomic DNA. Translation: ABE76004.1.
RefSeqiWP_011514537.1. NC_007969.1.
YP_581488.1. NC_007969.1.

3D structure databases

ProteinModelPortaliQ1Q8J9.
SMRiQ1Q8J9. Positions 1-717.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi335284.Pcryo_2227.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE76004; ABE76004; Pcryo_2227.
KEGGipcr:Pcryo_2227.
PATRICi23064087. VBIPsyCry128170_2356.

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000261344.
KOiK01825.
OMAiNWLEDGI.
OrthoDBiEOG6M9F0M.

Enzyme and pathway databases

UniPathwayiUPA00659.
BioCyciPCRY335284:GHE9-2271-MONOMER.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
HAMAPiMF_01621. FadB.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR02437. FadB. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of chromosome of Psychrobacter cryohalolentis K5."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J.
    , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.
    Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K5.

Entry informationi

Entry nameiFADB_PSYCK
AccessioniPrimary (citable) accession number: Q1Q8J9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: May 16, 2006
Last modified: June 24, 2015
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.